Evidence for CALM in directing VAMP2 trafficking

被引：115

作者：

Harel, Asaff ^{[1
]}

Wu, Fangbai ^{[1
]}

Mattson, Mark P. ^{[1
]}

Morris, Christa M. ^{[2
]}

Yao, Pamela J. ^{[1
]}

机构：

[1] NIA, Intramural Res Program, Neurosci Lab, Baltimore, MD 21224 USA

[2] NIA, Intramural Res Program, Flow Cytometry Lab, Baltimore, MD 21224 USA

来源：

TRAFFIC | 2008年 / 9卷 / 03期

关键词：

clathrin; endocytosis; flow cytometry; siRNA; SNARE proteins;

D O I：

10.1111/j.1600-0854.2007.00694.x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Clathrin assembly lymphoid myeloid leukemia protein (CALM) is a clathrin assembly protein with a domain structure similar to the neuron-specific assembly protein AP180. We have previously found that CALM is expressed in neurons and present in synapses. We now report that CALM has a neuron-related function: it facilitates the endocytosis of the synaptic vesicle protein VAMP2 from the plasma membrane. Overexpression of CALM leads to the reduction of cell surface VAMP2, whereas knockdown of CALM by RNA interference results in the accumulation of surface VAMP2. The AP180 N-terminal homology (ANTH) domain of CALM is required for its effect on VAMP2 trafficking, and the ANTH domain itself acts as a dominant-negative mutant. Thus, our results reveal a role for CALM in directing VAMP2 trafficking during endocytosis.

引用

页码：417 / 429

页数：13

共 43 条

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